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The Mitochondrial-Derived Peptide MOTS-c Promotes Metabolic Homeostasis and Reduces Obesity and Insulin Resistance
Open accessAbstract
Mitochondria are known to be functional organelles, but their role as a signaling unit is increasingly being appreciated. The identification of a short open reading frame (sORF) in the mitochondrial DNA (mtDNA) that encodes a signaling peptide, humanin, suggests the possible existence of additional sORFs in the mtDNA. Here we report a sORF within the mitochondrial 12S rRNA encoding a 16-amino-acid peptide named MOTS-c (mitochondrial open reading frame of the 12S rRNA-c) that regulates insulin sensitivity and metabolic homeostasis. Its primary target organ appears to be the skeletal muscle, and its cellular actions inhibit the folate cycle and its tethered de novo purine biosynthesis, leading to AMPK activation. MOTS-c treatment in mice prevented age-dependent and high-fat-diet-induced insulin resistance, as well as diet-induced obesity. These results suggest that mitochondria may actively regulate metabolic homeostasis at the cellular and organismal level via peptides encoded within their genome.
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“whilst recent studies have demonstrated that MOTS-c may also exert protective effects against diet-induced obesity and insulin resistance by altering skeletal muscle gene expression related to metabolism and inflammation”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [117]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Mitochondrial-derived peptides such as MOTS-c may further promote fatigue resistance and enhance muscle strength by activating key metabolic pathways and supporting mitochondrial health”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [117]
Experimental — accuracy not yet measuredIn the citing paper
“The mitochondrial open reading frame of the 12S rRNA-c (MOTS-c) is a bioactive mitochondrial-derived peptide shown to activate the AMPK pathway and modulate metabolic homeostasis [193].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [193]
In the citing paper
“Interestingly, treatment with MOTS-C in mice prevent agedependent and high-fat diet induced insulin resistance and obesity indicating an important role of mitochondria in the control of fat metabolism probably producing prolongevity effects (Fuku et al., 2015; Lee et al., 2015).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Lee et al., 2015
In the citing paper
“treatment with MOTS-C in mice prevent agedependent and high-fat diet induced insulin resistance and obesity indicating an important role of mitochondria in the control of fat metabolism probably producing prolongevity effects (Fuku et al., 2015; Lee et al., 2015).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Lee et al., 2015
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Cites
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049
Physiological Roles of Mitochondrial Reactive Oxygen Species
Sena, L. A., & Chandel, N. S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.025 · Cited by 2,632
Not So Different After All: A Comparison of Methods for Detecting Amino Acid Sites Under Selection
Pond, S. L. K., & Frost, S. D. W. (2005) · Molecular Biology and Evolution · doi:10.1093/molbev/msi105 · Cited by 2,320
Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,672
Price, N. L., Gomes, A. P., Ling, A. J. Y., Duarte, F. V., Martin-Montalvo, A., North, B. J., Agarwal, B., Ye, L., Ramadori, G., Teodoro, J. S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.003 · Cited by 1,602
Metformin improves healthspan and lifespan in mice
Martin-Montalvo, A., Mercken, E. M., Mitchell, S. J., Palacios, H. H., Mote, P. L., Scheibye-Knudsen, M., Gomes, A. P., Ward, T. M., Minor, R. K., Blouin, M.-J., et al. (2013) · Nature Communications · doi:10.1038/ncomms3192 · Cited by 1,445
Pearson, K. J., Baur, J. A., Lewis, K. N., Peshkin, L., Price, N. L., Labinskyy, N., Swindell, W. R., Kamara, D., Minor, R. K., Perez, E., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.06.011 · Cited by 1,162
Analysis of Microarray Data Using Z Score Transformation
Cheadle, C., Vawter, M. P., Freed, W. J., & Becker, K. G. (2003) · Journal of Molecular Diagnostics · doi:10.1016/s1525-1578(10)60455-2 · Cited by 1,150
Metabolism of Inflammation Limited by AMPK and Pseudo-Starvation
O'Neill, L. A. J., & Hardie, D. G. (2013) · Nature · doi:10.1038/nature11862 · Cited by 1,133
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Items 201–300 of 723
Systemic Regulators of Skeletal Muscle Regeneration in Obesity
Sinha, I., Sakthivel, D., & Varon, D. E. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00029 · Cited by 39
How do yeast sense mitochondrial dysfunction?
Кнорре, Д. А., Соколов, С. С., Zyrina, A. N., & Severin, F. F. (2016) · Microbial Cell · doi:10.15698/mic2016.11.537 · Cited by 39
Exogenous Bioactive Peptides Have a Potential Therapeutic Role in Delaying Aging in Rodent Models
Wang, J., Wu, Y., Chen, Z., Chen, Y., Lin, Q., & Liang, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031421 · Cited by 38
Mitochondrion: A bridge linking aging and degenerative diseases
Zhang, L., Wu, J., Zhu, Z., He, Y., & Fang, R. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121666 · Cited by 38
The Warburg effect: The hacked mitochondrial-nuclear communication in cancer
Jiang, H., & Ye, J. (2025) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2025.03.006 · Cited by 40
Xiao, J., Howard, L. E., Wan, J., Wiggins, E. K., Vidal, A. C., Cohen, P., & Freedland, S. J. (2017) · Oncotarget · doi:10.18632/oncotarget.20134 · Cited by 39
Self-citationLipids and insulin regulate mitochondrial‐derived peptide (MOTS‐c) in PCOS and healthy subjects
Ramanjaneya, M., Jerobin, J., Bettahi, I., Bensila, M., Aye, M., Siveen, K. S., Sathyapalan, T., Skarulis, M. C., Abou‐Samra, A., & Atkin, S. L. (2019) · Clinical Endocrinology · doi:10.1111/cen.14007 · Cited by 38
Role of Signaling Molecules in Mitochondrial Stress Response
Hill, S., Sataranatarajan, K., & Remmen, H. V. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00225 · Cited by 39
Mitochondrial biology and prostate cancer ethnic disparity
Xiao, J., Cohen, P., Stern, M. C., Odedina, F. T., Carpten, J. D., & Reams, R. (2018) · Carcinogenesis · doi:10.1093/carcin/bgy133 · Cited by 37
Self-citationUrban, C., Hayes, H. V., Piraino, G., Wolfe, V., Lahni, P. M., O’Connor, M. P., Phares, C., & Zingarelli, B. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.984298 · Cited by 37
Mitochondrial Stress and Mitokines: Therapeutic Perspectives for the Treatment of Metabolic Diseases
Zhang, B., Chang, J. Y., Lee, M. H., Ju, S. H., Yi, H., & Shong, M. (2024) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2023.0115 · Cited by 39
Mitochondrial genetics, signalling and stress responses
Liu, Y. J., Sulc, J., & Auwerx, J. H. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01625-w · Cited by 38
Peptides encoded by noncoding genes: challenges and perspectives
Wang, S., Mao, C., & Liu, S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0092-3 · Cited by 38
Dieli-Conwright, C. M., Sami, N., Norris, M. K., Wan, J., Kumagai, H., Kim, S., & Cohen, P. (2021) · Scientific Reports · doi:10.1038/s41598-021-96419-z · Cited by 36
Self-citationMOTS-c and Exercise Restore Cardiac Function by Activating of NRG1-ErbB Signaling in Diabetic Rats
Li, S., Wang, M., Ma, J., Pang, X., Yuan, J., Pan, Y., Fu, Y., & Laher, I. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.812032 · Cited by 36
Raijmakers, R. P. H., Jansen, A. F. M., Keijmel, S. P., ter Horst, R., Roerink, M. E., Novakovic, B., Joosten, L. A. B., van der Meer, J. W. M., Netea, M. G., & Bleeker‐Rovers, C. P. (2019) · Journal of Translational Medicine · doi:10.1186/s12967-019-1906-3 · Cited by 36
Skuratovskaia, D., Komar, A., Vulf, M. A., & Litvinova, L. S. (2020) · PeerJ · doi:10.7717/peerj.9741 · Cited by 37
Mitochondrial-Derived Peptides in Diabetes and Its Complications
Wu, Y., Sun, L., Zhuang, Z., Hu, X., & Dong, D. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.808120 · Cited by 35
Mitochondrial DNA: Consensuses and Controversies
Shokolenko, I. N., & ALEXEYEV, M. F. (2022) · DNA · doi:10.3390/dna2020010 · Cited by 35
Kumagai, H., Miller, B., Kim, S., Leelaprachakul, N., Kikuchi, N., Yen, K., & Cohen, P. (2023) · Genes · doi:10.3390/genes14020286 · Cited by 37
Self-citationKienzle, L., Bettinazzi, S., Choquette, T., Brunet, M. A., Khorami, H. H., Jacques, J., Moreau, M., Roucou, X., Landry, C. R., Angers, A., et al. (2023) · BMC Biology · doi:10.1186/s12915-023-01609-y · Cited by 39
Zhong, P., Peng, J., Hu, Y., Zhang, J., & Shen, C. (2022) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17551 · Cited by 34
Sulo, P., Szabóová, D., Bielik, P., Poláková, S., Šoltýs, K., Jatzová, K., & Szemes, T. (2017) · DNA Research · doi:10.1093/dnares/dsx026 · Cited by 34
Bravo, J. I., Nozownik, S., Danthi, P. S., & Benayoun, B. A. (2020) · Development · doi:10.1242/dev.175786 · Cited by 36
Mach, N., Moroldo, M., Rau, A., Lecardonnel, J., Moyec, L. L., Robert, C., & Barrey, É. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.656204 · Cited by 36
Shi, Y., Feng, R., Mao, J., Liu, S., Zhou, Z., Ji, Z., Chen, S., & Mao, J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.689092 · Cited by 34
Mitochondrial respiratory states and rates
Gnaiger, E., Frostner, E. Å., Karim, N. A., Abumrad, N. A., Castroviejo, D. A., Adiele, R. C., Ahn, B., Ali, S. S., Alton, L. A., Alves, M. G., et al. (2019) · Repository@Nottingham (University of Nottingham) · doi:10.26124/mitofit:190001 · Cited by 39
Li, M., Shao, F., Qian, Q., Yu, W., Zhang, Z., Chen, B., Su, D., Guo, Y., Phan, A.-V., Song, L., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.06.027 · Cited by 36
Effect of mitochondrial stress on systemic metabolism
Lee, M. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12822 · Cited by 32
Sreekumar, P. G., & Kannan, R. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101663 · Cited by 32
Humanin and diabetes mellitus: A review of in vitro and in vivo studies
Boutari, C., Pappas, P. D., Theodoridis, T. D., & Vavilis, D. (2022) · World Journal of Diabetes · doi:10.4239/wjd.v13.i3.213 · Cited by 36
Kim, K. H. (2023) · Theranostics · doi:10.7150/thno.84165 · Cited by 33
Kavak, A. G., Karslıoğlu, İ., Saracaloğlu, A., Demiryürek, Ş., & Demiryürek, A. T. (2024) · Current Radiopharmaceuticals · doi:10.2174/0118744710254730231114181358 · Cited by 31
An evolutionary, or “Mitocentric” perspective on cellular function and disease
Brown, J. A., Sammy, M. J., & Ballinger, S. W. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101568 · Cited by 31
Yuan, J., Wang, M., Pan, Y., Liang, M., Fu, Y., Duan, Y., Tang, M., Laher, I., & Li, S. (2021) · Scientific Reports · doi:10.1038/s41598-021-99568-3 · Cited by 31
Sang, Y., Liu, J., Wang, F., Luo, X., Chen, Z.-Q., Zhuang, S., & Zhu, Y. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.04.012 · Cited by 31
Kim, S. K., Tran, T. L., NamKoong, C., Choi, H. J., Chun, H. J., Lee, Y., Cheon, M., Chung, C., Hwang, J., Lim, H., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40082-7 · Cited by 31
Self-citationThe influence of transcript assembly on the proteogenomics discovery of microproteins
Ma, J., Saghatelian, A., & Shokhirev, M. N. (2018) · PLoS ONE · doi:10.1371/journal.pone.0194518 · Cited by 31
Zmynd17 controls muscle mitochondrial quality and whole‐body metabolism
Fujita, R., Yoshioka, K., Seko, D., Suematsu, T., Mitsuhashi, S., Senoo, N., Miura, S., Nishino, I., & Ono, Y. (2018) · The FASEB Journal · doi:10.1096/fj.201701264r · Cited by 31
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Gunawan, A. L., Liparulo, I., & Stahl, A. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00549-3 · Cited by 33
Hernández‐Aguilera, A., Fernández‐Arroyo, S., Cuyàs, E., Luciano‐Mateo, F., Cabré, N., Camps, J., López‐Miranda, J., Menéndez, J. A., & Joven, J. (2016) · Food and Chemical Toxicology · doi:10.1016/j.fct.2016.08.006 · Cited by 30
Cardon, T., Salzet, M., Franck, J., & Fournier, I. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.05.009 · Cited by 33
HIV-1 Tat and cocaine impact mitochondrial epigenetics: effects on DNA methylation
Doke, M., Jeganathan, V., McLaughlin, J. P., & Samikkannu, T. (2020) · Epigenetics · doi:10.1080/15592294.2020.1834919 · Cited by 30
Cold exposure alters lipid metabolism of skeletal muscle through HIF-1α-induced mitophagy
Chen, W., Xu, Z., You, W., Zhou, Y., Wang, L., Huang, Y., & Shan, T. (2023) · BMC Biology · doi:10.1186/s12915-023-01514-4 · Cited by 31
Tang, M., Su, Q., Duan, Y., Fu, Y., Liang, M., Pan, Y., Yuan, J., Wang, M., Pang, X., Ma, J., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-47073-0 · Cited by 29
A large-scale sORF screen identifies putative microproteins involved in cancer cell fitness
Schlesinger, D., Dirks, C., Navarro, C., Lafranchi, L., Spinner, A., Arul, G. L. R., Tong, G. M.-S., Eirich, J., Martinez, T. F., & Elsässer, S. J. (2025) · iScience · doi:10.1016/j.isci.2025.111884 · Cited by 32
Minireview: Novel Micropeptide Discovery by Proteomics and Deep Sequencing Methods
Tharakan, R., & Sawa, A. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.651485 · Cited by 29
UPRmt and coordinated UPRER in type 2 diabetes
Kang, Z., Chen, F., Wu, W., Liu, R. R., Chen, T., & Xu, F. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.974083 · Cited by 29
Inter-tissue communication of mitochondrial stress and metabolic health
Zhang, H., Li, X., Fan, W., Pandovski, S., Tian, Y., & Dillin, A. G. (2023) · Life Metabolism · doi:10.1093/lifemeta/load001 · Cited by 30
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Gao, Y., Wei, X., Wei, P., Lu, H., Zhong, L., Tan, J., Liu, H., & Liu, Z. (2023) · Metabolites · doi:10.3390/metabo13010125 · Cited by 30
Wu, J., Xiao, D., Yu, K., Shalamu, K., He, B., & Zhang, M. (2023) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2023006 · Cited by 29
Jiang, J., Xu, L., Yang, L., Liu, S., & Wang, Z. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00140 · Cited by 29
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Wang, Y., Li, J., Zhang, Z., Wang, R., Hai, B., & Zhang, Y. (2023) · Life · doi:10.3390/life13041006 · Cited by 29
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Cruz‐Bermúdez, A., Vicente-Blanco, R. J., González‐Vioque, E., Provencio, M., Fernández‐Moreno, M. Á., & Garesse, R. (2016) · Clinical & Translational Oncology · doi:10.1007/s12094-016-1561-6 · Cited by 29
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Picca, A., Guerra, F., Calvani, R., Romanò, R., Coelho‐Júnior, H. J., Bucci, C., Leeuwenburgh, C., & Marzetti, E. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.023 · Cited by 28
Li, N., Zhou, Y., Wang, J., Niu, L., Zhang, Q., Sun, L., Ding, X. D., Guo, X., Xie, Z., Zhu, N., et al. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00232 · Cited by 30
Pliouta, L., Lampsas, S., Kountouri, A., Korakas, E., Thymis, J., Kassi, E. N., Oikonomou, E. K., Ikonomidis, I., & Lambadiari, V. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14113706 · Cited by 27
Sequeira, I. R., Woodhead, J. S. T., Chan, A., D’Souza, R. F., Wan, J., Hollingsworth, K. G., Plank, L. D., Cohen, P., Poppitt, S. D., & Merry, T. L. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129991 · Cited by 27
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Self-citationJiang, J., Chang, X., Nie, Y., Xu, L., Yang, L., Peng, Y., & Chang, M. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175469 · Cited by 27
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Chothani, S. P., Ho, L., Schäfer, S., & Rackham, O. J. L. (2023) · RNA Biology · doi:10.1080/15476286.2023.2279845 · Cited by 27
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Zanet, J., Chanut-Delalande, H., Plaza, S., & Payre, F. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2015.11.004 · Cited by 30
Mitochondrial-derived microproteins: from discovery to function
Yen, K., Miller, B., Kumagai, H., Silverstein, A. R., & Cohen, P. (2024) · Trends in Genetics · doi:10.1016/j.tig.2024.11.010 · Cited by 25
Self-citationMOTS-c repairs myocardial damage by inhibiting the CCN1/ERK1/2/EGR1 pathway in diabetic rats
Wang, M., Wang, G., Pang, X., Ma, J., Yuan, J., Pan, Y., Fu, Y., Laher, I., & Li, S. (2023) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1060684 · Cited by 25
Lü, P., Li, X., Li, B., Li, X., Wang, C., Liu, Z., Ji, Y., Wang, X., Wen, Z., Fan, J., et al. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175835 · Cited by 25
Miller, B., Arpawong, T. E., Jiao, H., Kim, S., Yen, K., Mehta, H. H., Wan, J., Carpten, J. D., & Cohen, P. (2019) · Cells · doi:10.3390/cells8040306 · Cited by 25
Self-citationLin, C., Luo, L., Xun, Z., Zhu, C., Huang, Y., Ye, Y., Zhang, J., Chen, T., Wu, S., Zhan, F., et al. (2023) · Gut · doi:10.1136/gutjnl-2023-330389 · Cited by 25
Zhang, Y., Gao, Y., Wang, J.-R., Gao, R., Su, Q., Ju, Z., Jiang, L., Zhang, C., Huang, P., Wang, W., et al. (2024) · Advanced Functional Materials · doi:10.1002/adfm.202312772 · Cited by 24
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Darwish, R., Alcibahy, Y., Abu-Sharia, G., & Butler, A. E. (2025) · Cells · doi:10.3390/cells14231861 · Cited by 25
Lee, D. E., Brown, J. L., Rosa, M. E., Brown, L. A., Perry, R. A., Washington, T. A., & Greene, N. P. (2016) · Acta Physiologica · doi:10.1111/apha.12687 · Cited by 28
Baylan, F. A., & Yarar, E. (2021) · Sleep And Breathing · doi:10.1007/s11325-020-02273-0 · Cited by 25
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Self-citationNewell, C., Hume, S. L., Greenway, S. C., Podemski, L., Shearer, J., & Khan, A. (2018) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2018.10.002 · Cited by 24
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Veloso, C. D., Belew, G. D., Ferreira, L. L., Grilo, L. F., Jones, J. G., Portincasa, P., Sardão, V. A., & Oliveira, P. J. (2019) · Current Pharmaceutical Design · doi:10.2174/1389203720666190830163735 · Cited by 24
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Metadata
- Authors
- Lee, C., Zeng, J., Drew, B. G., Sallam, T., Martin-Montalvo, A., Wan, J., Kim, S.-J., Mehta, H., Hevener, A. L., de Cabo, R., & Cohen, P.
- Affiliations
- University of Southern California (US)
- University of California, Los Angeles (US)
- Corresponding author
- Lee, Changhan
- Cohen, Pinchas
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2015-03
- Volume
- 21
- Issue
- 3
- Pages
- 443-454
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4350682
- OpenAlex
- W2160343816
- Cited by
- 715
- References
- 62
- Citations by year
- 2026: 61 · 2025: 77 · 2024: 104 · 2023: 97 · 2022: 59 · 2021: 67 · 2020: 68 · 2019: 55 · 2018: 45 · 2017: 27 · 2016: 40 · 2015: 15
- FWCI
- 18.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (UL1TR000130, 7r01ag034430-05)
- National Institute on Aging (1R01AG 034430, # R01AG034430)
- National Institute of General Medical Sciences (R01GM090311)
- National Institute of Diabetes and Digestive and Kidney Diseases (NIH DK063491, P30DK063491)
- National Institute of Environmental Health Sciences (R01ES020812)
- National Center for Advancing Translational Sciences
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- MOTS-c, mitochondrial peptides, 12S rRNA, small open reading frames, mitochondrial DNA, metabolic homeostasis, insulin resistance, obesity, AMPK activation, folate cycle, de novo purine synthesis, skeletal muscle, mitochondrial signaling
- MeSH terms
- Animals, Cell Line, DNA, Mitochondrial, HeLa Cells, Homeostasis, Humans, Insulin, Insulin Resistance, Male, Mice, Inbred C57BL, Mice, Inbred ICR, Mitochondria, Obesity, Peptides, Signal Transduction, Muscle, Skeletal, Cell Line, Tumor, Mice, AMP-Activated Protein Kinases, HEK293 Cells, Diet, High-Fat
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